Premium
RING finger protein 38 induces gastric cancer cell growth by decreasing the stability of the protein tyrosine phosphatase SHP ‐1
Author(s) -
Zhang Jigang,
Wu Hao,
Yi Bin,
Zhou Jian,
Wei Luxin,
Chen Yan,
Zhang Lifeng
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13225
Subject(s) - protein tyrosine phosphatase , cancer , cancer research , ubiquitin ligase , downregulation and upregulation , cancer cell , cell growth , chemistry , gene silencing , tyrosine , phosphatase , ptpn11 , tyrosine kinase , ubiquitin , signal transduction , biology , phosphorylation , microbiology and biotechnology , biochemistry , genetics , gene , colorectal cancer , kras
The function of the E3 ligase RNF 38 is still unknown in gastric cancer. Here, we found that RNF 38 is upregulated in gastric cancer, and it is associated with the overall survival of gastric cancer patients. Further studies showed that RNF 38 interacts with the nonreceptor tyrosine phosphatase SH 2‐containing protein tyrosine phosphatase 1 ( SHP ‐1) and induces the polyubiquitination of SHP ‐1, which leads to destabilization of SHP ‐1 and promotion of STAT 3 signaling in gastric cancer cells. In addition, overexpression or knockdown of RNF 38 induces or suppresses gastric cancer cell growth in vitro , respectively, and silencing RNF 38 delays tumor growth in vivo . These findings demonstrate that RNF 38 is functional in gastric cancer and promotes STAT 3 signaling by destabilizing SHP ‐1; thus, RNF 38 could be a novel target for gastric cancer therapy.